GenomeNet

Database: UniProt
Entry: A3TPN7_9MICO
LinkDB: A3TPN7_9MICO
Original site: A3TPN7_9MICO 
ID   A3TPN7_9MICO            Unreviewed;       478 AA.
AC   A3TPN7;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   24-JAN-2024, entry version 79.
DE   RecName: Full=GMP reductase {ECO:0000256|HAMAP-Rule:MF_02250};
DE            EC=1.7.1.7 {ECO:0000256|HAMAP-Rule:MF_02250};
DE   AltName: Full=Guanosine 5'-monophosphate reductase {ECO:0000256|HAMAP-Rule:MF_02250};
DE            Short=GMPR {ECO:0000256|HAMAP-Rule:MF_02250};
GN   Name=guaB1 {ECO:0000256|HAMAP-Rule:MF_02250};
GN   ORFNames=JNB_16063 {ECO:0000313|EMBL:EAP98495.1};
OS   Janibacter sp. HTCC2649.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Janibacter.
OX   NCBI_TaxID=313589 {ECO:0000313|EMBL:EAP98495.1, ECO:0000313|Proteomes:UP000005063};
RN   [1] {ECO:0000313|EMBL:EAP98495.1, ECO:0000313|Proteomes:UP000005063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2649 {ECO:0000313|EMBL:EAP98495.1,
RC   ECO:0000313|Proteomes:UP000005063};
RX   PubMed=21075932; DOI=10.1128/JB.01298-10;
RA   Thrash J.C., Cho J.C., Bertagnolli A.D., Ferriera S., Johnson J.,
RA   Vergin K.L., Giovannoni S.J.;
RT   "Genome sequence of the Marine Janibacter Sp. Strain HTCC2649.";
RL   J. Bacteriol. 193:584-585(2011).
CC   -!- FUNCTION: Involved in the purine-salvage pathway. Catalyzes the NADPH-
CC       dependent conversion of GMP to IMP. {ECO:0000256|HAMAP-Rule:MF_02250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=IMP + NADP(+) + NH4(+) = GMP + 2 H(+) + NADPH;
CC         Xref=Rhea:RHEA:17185, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58053, ChEBI:CHEBI:58115,
CC         ChEBI:CHEBI:58349; EC=1.7.1.7; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_02250};
CC   -!- COFACTOR:
CC       Name=a monovalent cation; Xref=ChEBI:CHEBI:60242;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02250};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway.
CC       {ECO:0000256|HAMAP-Rule:MF_02250}.
CC   -!- SIMILARITY: Belongs to the IMPDH/GMPR family. GuaB1 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_02250}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAP98495.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AAMN01000003; EAP98495.1; -; Genomic_DNA.
DR   RefSeq; WP_009777500.1; NZ_CH672413.1.
DR   AlphaFoldDB; A3TPN7; -.
DR   STRING; 313589.JNB_16063; -.
DR   eggNOG; COG0516; Bacteria.
DR   eggNOG; COG0517; Bacteria.
DR   HOGENOM; CLU_022552_2_1_11; -.
DR   OrthoDB; 9805398at2; -.
DR   Proteomes; UP000005063; Unassembled WGS sequence.
DR   GO; GO:0003920; F:GMP reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003938; F:IMP dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:InterPro.
DR   GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
DR   CDD; cd02205; CBS_pair_SF; 1.
DR   CDD; cd00381; IMPDH; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_02250; GMPR_GuaB1; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000644; CBS_dom.
DR   InterPro; IPR046342; CBS_dom_sf.
DR   InterPro; IPR005991; GUAB1.
DR   InterPro; IPR005990; IMP_DH.
DR   InterPro; IPR001093; IMP_DH_GMPRt.
DR   NCBIfam; TIGR01303; IMP_DH_rel_1; 1.
DR   PANTHER; PTHR43170; GMP REDUCTASE; 1.
DR   PANTHER; PTHR43170:SF5; GMP REDUCTASE; 1.
DR   Pfam; PF00571; CBS; 2.
DR   Pfam; PF00478; IMPDH; 1.
DR   PIRSF; PIRSF000130; IMPDH; 1.
DR   SMART; SM00116; CBS; 2.
DR   SMART; SM01240; IMPDH; 1.
DR   SUPFAM; SSF54631; CBS-domain pair; 1.
DR   SUPFAM; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 1.
DR   PROSITE; PS51371; CBS; 1.
PE   3: Inferred from homology;
KW   CBS domain {ECO:0000256|ARBA:ARBA00023122, ECO:0000256|PROSITE-
KW   ProRule:PRU00703}; NAD {ECO:0000256|PIRSR:PIRSR000130-3};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_02250};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_02250};
KW   Potassium {ECO:0000256|PIRSR:PIRSR000130-4};
KW   Purine salvage {ECO:0000256|ARBA:ARBA00022726, ECO:0000256|HAMAP-
KW   Rule:MF_02250}; Reference proteome {ECO:0000313|Proteomes:UP000005063}.
FT   DOMAIN          153..209
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   ACT_SITE        302
FT                   /note="Thioimidate intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02250"
FT   BINDING         245..247
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000130-3"
FT   BINDING         245..247
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02250"
FT   BINDING         295..297
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000130-3"
FT   BINDING         295..297
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02250"
FT   BINDING         297
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_note="ligand shared between two tetrameric
FT                   partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000130-4"
FT   BINDING         299
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_note="ligand shared between two tetrameric
FT                   partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000130-4"
FT   BINDING         302
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_note="ligand shared between two tetrameric
FT                   partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000130-4"
SQ   SEQUENCE   478 AA;  50715 MW;  0C1E2B0EB76FD683 CRC64;
     MHFLNDLQPQ FDLTYDDVFM VPNQSDVTSR LDVDLSSDDG TGTTIPLVVA NMTAIAGRRM
     AETTARRGAL TIIPQDIPRD VVSEVIGWTK QRHLVFDTAI TLDPHTTVGE AQVLIGKRAH
     GAAVVTEAGL PIGVVTEKDL GGVDRFVQVR DVMSRELVTV RDDVDVVRAF DTLNESRRRL
     APVVAADGTL VGVLTRLGAL RANLYSPAVD ANGALRIGAA VGINGDVAAK ASQLLEAGAD
     VLVIDTAHGH QQKMLDALRA VRDLDPQVPI VAGNVVSAAG TRALIEAGAD IVKVGVGPGA
     MCTTRMMTAV GRPQFSAVLE CATAAGELGK HVWADGGVRH PRDVALALAA GASNVMIGSW
     FAGTLESPGD LFSDEKGRQF KESFGMASSR AVRNRTATDT AYERARKAMF EEGISSARMF
     IDPARPSVED VIDEIIAGLR SSCTYAGART LGEYHERATV GIQSTAGFAE GRPLHQSW
//
DBGET integrated database retrieval system